The inhibition of human neutrophil elastase and cathepsin G by peptidyl 1,2-dicarbonyl derivatives |
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Authors: | S Mehdi M R Angelastro J P Burkhart J R Koehl N P Peet P Bey |
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Affiliation: | Merrell Dow Research Institute, Cincinnati, OH 45215. |
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Abstract: | Neutrophil elastase and cathepsin G are serine proteases that can damage connective tissue and trigger other pathological reactions. Compounds containing a peptide sequence to impart specificity and bearing an alpha-dicarbonyl unit (alpha-diketone or alpha-keto ester) at the carboxy terminus are potent inhibitors of the neutrophil serine proteases (human neutrophil elastase: R-Val-COCH3, Ki = 0.017 microM; R-Val-COOCH3, Ki = 0.002 microM; human neutrophil cathepsin G: R-Phe-COCH3, Ki = 0.8 microM; R-Phe-COOCH3, Ki = 0.44 microM; R = N-(4-[(4-chlorophenyl)sulfonylaminocarbonyl]phenylcarbonyl)+ ++ValylProlyl). |
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